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Volumn , Issue , 2010, Pages 59-87

Nuclear Magnetic Resonance Spectroscopy Applied to (Intrinsically) Disordered Proteins

Author keywords

Molecular alignment and RDCs; Multidimensional NMR and isotopic enrichment; Spectroscopic techniques nuclear magnetic resonance spectroscopy for disordered proteins

Indexed keywords


EID: 84885501621     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470602614.ch3     Document Type: Chapter
Times cited : (3)

References (42)
  • 2
    • 0036815758 scopus 로고    scopus 로고
    • NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis
    • Akke, M. 2002. NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis. Curr Opin Struct Biol 12: 642-7.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 642-647
    • Akke, M.1
  • 3
    • 16244388547 scopus 로고    scopus 로고
    • Rapid NMR data collection
    • Atreya, H. S., and T. Szyperski. 2005. Rapid NMR data collection. Methods Enzymol 394: 78-108.
    • (2005) Methods Enzymol , vol.394 , pp. 78-108
    • Atreya, H.S.1    Szyperski, T.2
  • 4
    • 4744349987 scopus 로고    scopus 로고
    • Combining prediction, computation and experiment for the characterization of protein disorder
    • Bracken, C., L. M. Iakoucheva, P. R. Rorner, and A. K. Dunker. 2004. Combining prediction, computation and experiment for the characterization of protein disorder . Curr Opin Struct Biol 14: 570-6.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 570-576
    • Bracken, C.1    Iakoucheva, L.M.2    Rorner, P.R.3    Dunker, A.K.4
  • 5
    • 0000084729 scopus 로고
    • Sequence - corrected N - 15 random coil chemical - shifts
    • Braun, D., G. Wider, and K. Wuthrich. 1994. Sequence - corrected N - 15 random coil chemical - shifts. J Am Chem Soc 116: 8466-9.
    • (1994) J Am Chem Soc , vol.116 , pp. 8466-8469
    • Braun, D.1    Wider, G.2    Wuthrich, K.3
  • 6
    • 0033595571 scopus 로고    scopus 로고
    • Dynamics of unfolded proteins: incorporation of distributions of correlation times in the model free analysis of NMR relaxation data
    • Buevich, A. V., and J. Baum. 1999. Dynamics of unfolded proteins: incorporation of distributions of correlation times in the model free analysis of NMR relaxation data. J Am Chem Soc 121: 8671-2.
    • (1999) J Am Chem Soc , vol.121 , pp. 8671-8672
    • Buevich, A.V.1    Baum, J.2
  • 7
    • 0036283096 scopus 로고    scopus 로고
    • Molecular dynamics and NMR spin relaxation in proteins
    • Case, D. A. 2002. Molecular dynamics and NMR spin relaxation in proteins. Acc Chem Res 35: 325-31.
    • (2002) Acc Chem Res , vol.35 , pp. 325-331
    • Case, D.A.1
  • 10
    • 0036300690 scopus 로고    scopus 로고
    • Distribution of molecular size within an unfolded state ensemble using small - angle X - ray scattering and pulse field gradient NMR techniques
    • Choy, W. Y., F. A. A. Mulder, K. A. Crowhurst, D. R. Muhandiram, I. S. Millett, S. Doniach, J. D. Forman - Kay, and L. E. Kay. 2002. Distribution of molecular size within an unfolded state ensemble using small - angle X - ray scattering and pulse field gradient NMR techniques. J Mol Biol 316: 101-12.
    • (2002) J Mol Biol , vol.316 , pp. 101-112
    • Choy, W.Y.1    Mulder, F.A.A.2    Crowhurst, K.A.3    Muhandiram, D.R.4    Millett, I.S.5    Doniach, S.6    Forman-Kay, J.D.7    Kay, L.E.8
  • 11
    • 0030330918 scopus 로고    scopus 로고
    • Insights into protein folding from NMR
    • Dyson, H. J., and P. E. Wright. 1996. Insights into protein folding from NMR. Annu Rev Phys Chem 47: 369-95.
    • (1996) Annu Rev Phys Chem , vol.47 , pp. 369-395
    • Dyson, H.J.1    Wright, P.E.2
  • 12
    • 0036400715 scopus 로고    scopus 로고
    • Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance
    • Dyson, H. J., and P. E. Wright. 2002. Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance. Adv Protein Chem 62: 311-40.
    • (2002) Adv Protein Chem , vol.62 , pp. 311-340
    • Dyson, H.J.1    Wright, P.E.2
  • 13
    • 0034912536 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states
    • Dyson, H. J., and P. E. Wright. 2001. Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states. Methods Enzymol 339: 258-70.
    • (2001) Methods Enzymol , vol.339 , pp. 258-270
    • Dyson, H.J.1    Wright, P.E.2
  • 14
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson, H. J., and P. E. Wright. 2004. Unfolded proteins and protein folding studied by NMR. Chem Rev 104: 3607-22.
    • (2004) Chem Rev , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 17
    • 0029437296 scopus 로고
    • Pulsed field gradient multi - dimensional NMR methods for the study of protein structure and dynamics in solution
    • Kay, L. E. 1995. Pulsed field gradient multi - dimensional NMR methods for the study of protein structure and dynamics in solution. Prog Biophys Mol Biol 63: 277-99.
    • (1995) Prog Biophys Mol Biol , vol.63 , pp. 277-299
    • Kay, L.E.1
  • 19
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • Kosen, P. A. 1989. Spin labeling of proteins. Methods Enzymol 177: 86-121.
    • (1989) Methods Enzymol , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 21
    • 0003420010 scopus 로고    scopus 로고
    • Spin Dynamics. Basics of Nuclear Magnetic Resonance
    • John Wiley & Sons, Chichester, UK
    • Levitt, M. H. 2001. Spin Dynamics. Basics of Nuclear Magnetic Resonance. John Wiley & Sons, Chichester, UK.
    • (2001)
    • Levitt, M.H.1
  • 22
    • 19944411144 scopus 로고    scopus 로고
    • High - throughput analysis of protein NMR spectra
    • Malmodin, D., and M. Billeter. 2005. High - throughput analysis of protein NMR spectra. Prog Nucl Magn Reson Spectrosc 46: 109-29.
    • (2005) Prog Nucl Magn Reson Spectrosc , vol.46 , pp. 109-129
    • Malmodin, D.1    Billeter, M.2
  • 23
    • 41449109638 scopus 로고    scopus 로고
    • Conformational distributions of unfolded polypeptides from novel NMR techniques
    • Meier, S., M. Blackledge, and S. Grzesiek. 2008. Conformational distributions of unfolded polypeptides from novel NMR techniques. J Chem Phys 128: 052204.
    • (2008) J Chem Phys , vol.128 , pp. 052204
    • Meier, S.1    Blackledge, M.2    Grzesiek, S.3
  • 24
    • 55649093500 scopus 로고    scopus 로고
    • Model - independent interpretation of NMR relaxation data for unfolded proteins: the acid - denatured state of ACBP
    • Modig, K., and F. M. Poulsen. 2008. Model - independent interpretation of NMR relaxation data for unfolded proteins: the acid - denatured state of ACBP. J Biomol NMR 42: 163-77.
    • (2008) J Biomol NMR , vol.42 , pp. 163-177
    • Modig, K.1    Poulsen, F.M.2
  • 25
    • 0036127432 scopus 로고    scopus 로고
    • Dynamical characterization of residual and non - native structures in a partially folded protein by N - 15 NMR relaxation using a model based on a distribution of correlation times
    • Ochsenbein, F., J. M. Neumann, E. Guittet, and C. Van Heijenoort. 2002. Dynamical characterization of residual and non - native structures in a partially folded protein by N - 15 NMR relaxation using a model based on a distribution of correlation times. Protein Sci 11: 957-64.
    • (2002) Protein Sci , vol.11 , pp. 957-964
    • Ochsenbein, F.1    Neumann, J.M.2    Guittet, E.3    Van Heijenoort, C.4
  • 26
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond - to - millisecond motions in biological macromolecules
    • Palmer, A. G., C. D. Kroenke, and J. P. Loria. 2001. Nuclear magnetic resonance methods for quantifying microsecond - to - millisecond motions in biological macromolecules . Methods Enzymol 339: 204-38.
    • (2001) Methods Enzymol , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 27
    • 4344648452 scopus 로고    scopus 로고
    • Residual dipolar couplings in structure determination of biomolecules
    • Prestegard, J. H., C. M. Bougault, and A. I. Kishore. 2004. Residual dipolar couplings in structure determination of biomolecules. Chem Rev 104: 3519-40.
    • (2004) Chem Rev , vol.104 , pp. 3519-3540
    • Prestegard, J.H.1    Bougault, C.M.2    Kishore, A.I.3
  • 28
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler, M., J. Schleucher, and C. Griesinger. 1999. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog Nucl Magn Reson Spectrosc 34: 93-158.
    • (1999) Prog Nucl Magn Reson Spectrosc , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 31
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non - native states of proteins by NMR methods
    • Shortle, D. R. 1996. Structural analysis of non - native states of proteins by NMR methods. Curr Opin Struct Biol 6: 24-30.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 24-30
    • Shortle, D.R.1
  • 33
    • 0027482556 scopus 로고
    • Nmr relaxation and protein mobility
    • Wagner, G. 1993. Nmr relaxation and protein mobility. Curr Opin Struct Biol 3: 748-54.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 748-754
    • Wagner, G.1
  • 34
    • 0037184476 scopus 로고    scopus 로고
    • Investigation of the neighboring residue effects on protein chemical shifts
    • Wang, Y. J., and O. Jardetzky. 2002. Investigation of the neighboring residue effects on protein chemical shifts. J Am Chem Soc 124: 14075-84.
    • (2002) J Am Chem Soc , vol.124 , pp. 14075-84
    • Wang, Y.J.1    Jardetzky, O.2
  • 35
    • 0000961515 scopus 로고    scopus 로고
    • Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution
    • Wider, G. 1998. Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution. Prog Nucl Magn Reson Spectrosc 32: 193-275.
    • (1998) Prog Nucl Magn Reson Spectrosc , vol.32 , pp. 193-275
    • Wider, G.1
  • 36
    • 84888743437 scopus 로고    scopus 로고
    • Conformation and dynamics of nonnative states of proteins studied by NMR spectroscopy, pp. 737-808. In J. Buchner and T. Kiefhaber (eds.), Protein Folding Handbook
    • Wirmer, J., C. Schl ö rb, and H. Schwalbe. 2005. Conformation and dynamics of nonnative states of proteins studied by NMR spectroscopy, pp. 737-808. In J. Buchner and T. Kiefhaber (eds.), Protein Folding Handbook. Part I. Wiley - VCH, Weinheim, Germany.
    • (2005) Part I. Wiley - VCH, Weinheim, Germany
    • Wirmer, J.1    Schlörb, C.2    Schwalbe, H.3
  • 38
    • 0028673594 scopus 로고
    • Chemical - shifts as a tool for structure determination
    • Wishart, D. S., and B. D. Sykes. 1994. Chemical - shifts as a tool for structure determination . Nucl Magn Reson 239: 363-92.
    • (1994) Nucl Magn Reson , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 39
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re - assessing the protein structure - function paradigm
    • Wright, P. E., and H. J. Dyson. 1999. Intrinsically unstructured proteins: re - assessing the protein structure - function paradigm. J Mol Biol 293: 321-31.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 42
    • 0031451750 scopus 로고    scopus 로고
    • Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins
    • Yao, J., H. J. Dyson, and P. E. Wright. 1997. Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins. FEBS Lett 419: 285-9.
    • (1997) FEBS Lett , vol.419 , pp. 285-289
    • Yao, J.1    Dyson, H.J.2    Wright, P.E.3


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